Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods
Effect of temperature and pH on the interaction of curcumin with β-casein was explored by fluorescence spectroscopy, ultraviolet-visible spectroscopy and molecular dynamics simulation. The spectroscopic results showed that curcumin could bind to β-casein to form a complex which was driven mainly by...
Main Authors: | , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2021-08-01
|
Series: | Molecules |
Subjects: | |
Online Access: | https://www.mdpi.com/1420-3049/26/16/5092 |
id |
doaj-8930c0f63b6649708b5b4d360b4ba46f |
---|---|
record_format |
Article |
spelling |
doaj-8930c0f63b6649708b5b4d360b4ba46f2021-08-26T14:08:23ZengMDPI AGMolecules1420-30492021-08-01265092509210.3390/molecules26165092Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation MethodsRuichen Zhao0Xiaoli Qin1Jinfeng Zhong2College of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaEffect of temperature and pH on the interaction of curcumin with β-casein was explored by fluorescence spectroscopy, ultraviolet-visible spectroscopy and molecular dynamics simulation. The spectroscopic results showed that curcumin could bind to β-casein to form a complex which was driven mainly by electrostatic interaction. The intrinsic fluorescence of β-casein was quenched by curcumin through static quenching mechanism. The binding constants of curcumin to β-casein were 6.48 × 10<sup>4</sup> L/mol (298 K), 6.17 × 10<sup>4</sup> L/mol (305 K) and 5.73 × 10<sup>4</sup> L/mol (312 K) at pH 2.0, which was greater than that (3.98 × 10<sup>4</sup> L/mol at 298 K, 3.90 × 10<sup>4</sup> L/mol at 305 K and 3.41 × 10<sup>4</sup> L/mol at 312 K) at pH 7.4. Molecular docking study showed that binding energy of β-casein-curcumin complex at pH 2.0 (−7.53 kcal/mol) was lower than that at pH 7.4 (−7.01 kcal/mol). The molecular dynamics simulation study showed that the binding energy (−131.07 kJ/mol) of β-casein-curcumin complex was relatively low at pH 2.0 and 298 K. α-Helix content in β-casein was decreased and random coil content was increased in the presence of curcumin. These results can promote a deep understanding of interaction between curcumin and β-casein and provide a reference for improving the bioavailability of curcumin.https://www.mdpi.com/1420-3049/26/16/5092hydrophobic interactionfluorescence quenchingmolecular dockingsecondary structure contentthermodynamic parameters |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Ruichen Zhao Xiaoli Qin Jinfeng Zhong |
spellingShingle |
Ruichen Zhao Xiaoli Qin Jinfeng Zhong Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods Molecules hydrophobic interaction fluorescence quenching molecular docking secondary structure content thermodynamic parameters |
author_facet |
Ruichen Zhao Xiaoli Qin Jinfeng Zhong |
author_sort |
Ruichen Zhao |
title |
Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods |
title_short |
Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods |
title_full |
Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods |
title_fullStr |
Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods |
title_full_unstemmed |
Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods |
title_sort |
interaction between curcumin and β-casein: multi-spectroscopic and molecular dynamics simulation methods |
publisher |
MDPI AG |
series |
Molecules |
issn |
1420-3049 |
publishDate |
2021-08-01 |
description |
Effect of temperature and pH on the interaction of curcumin with β-casein was explored by fluorescence spectroscopy, ultraviolet-visible spectroscopy and molecular dynamics simulation. The spectroscopic results showed that curcumin could bind to β-casein to form a complex which was driven mainly by electrostatic interaction. The intrinsic fluorescence of β-casein was quenched by curcumin through static quenching mechanism. The binding constants of curcumin to β-casein were 6.48 × 10<sup>4</sup> L/mol (298 K), 6.17 × 10<sup>4</sup> L/mol (305 K) and 5.73 × 10<sup>4</sup> L/mol (312 K) at pH 2.0, which was greater than that (3.98 × 10<sup>4</sup> L/mol at 298 K, 3.90 × 10<sup>4</sup> L/mol at 305 K and 3.41 × 10<sup>4</sup> L/mol at 312 K) at pH 7.4. Molecular docking study showed that binding energy of β-casein-curcumin complex at pH 2.0 (−7.53 kcal/mol) was lower than that at pH 7.4 (−7.01 kcal/mol). The molecular dynamics simulation study showed that the binding energy (−131.07 kJ/mol) of β-casein-curcumin complex was relatively low at pH 2.0 and 298 K. α-Helix content in β-casein was decreased and random coil content was increased in the presence of curcumin. These results can promote a deep understanding of interaction between curcumin and β-casein and provide a reference for improving the bioavailability of curcumin. |
topic |
hydrophobic interaction fluorescence quenching molecular docking secondary structure content thermodynamic parameters |
url |
https://www.mdpi.com/1420-3049/26/16/5092 |
work_keys_str_mv |
AT ruichenzhao interactionbetweencurcuminandbcaseinmultispectroscopicandmoleculardynamicssimulationmethods AT xiaoliqin interactionbetweencurcuminandbcaseinmultispectroscopicandmoleculardynamicssimulationmethods AT jinfengzhong interactionbetweencurcuminandbcaseinmultispectroscopicandmoleculardynamicssimulationmethods |
_version_ |
1721191123048726528 |